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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

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Selective chemical protein modification.

Christopher D Spicer1, Benjamin G Davis1

  • 1Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford OX1 3TA, UK.

Nature Communications
|September 6, 2014
PubMed
Summary
This summary is machine-generated.

Protein chemical modification enables new tools for biology and medicine. Advances provide a versatile toolkit for site-selective reactions on amino acids, expanding possibilities for synthetic biology applications.

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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
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Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Chemical Biology

Background:

  • Protein chemical modification is crucial for biological research, therapeutics, and novel protein design.
  • Site-selective reactions demand precise control over chemo- and regioselectivity under physiological conditions.
  • Historically, modification was limited to cysteine and lysine residues.

Purpose of the Study:

  • To review the advancements in site-selective protein modification chemistry.
  • To highlight the expanding 'toolkit' for modifying amino acids.
  • To discuss the potential of these methods for synthetic biology.

Main Methods:

  • Review of literature on chemical modification of proteins.
  • Analysis of methods for site-selective reactions on natural and unnatural amino acids.
  • Discussion of biologically benign reaction conditions.

Main Results:

  • A diverse 'toolkit' of chemical modification methods is now available.
  • These methods offer control over chemo- and regioselectivity.
  • The toolkit has expanded beyond traditional cysteine and lysine modifications.

Conclusions:

  • Site-selective protein modification chemistry has significantly advanced.
  • These advancements provide powerful tools for biological applications.
  • Biologically benign application of this chemistry can enable true synthetic biology.